U3IP2_HUMAN
ID U3IP2_HUMAN Reviewed; 475 AA.
AC O43818; B2R996; Q8IZ30;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=U3 small nucleolar RNA-interacting protein 2;
DE AltName: Full=RRP9 homolog;
DE AltName: Full=U3 small nucleolar ribonucleoprotein-associated 55 kDa protein {ECO:0000303|PubMed:26867678};
DE Short=U3 snoRNP-associated 55 kDa protein {ECO:0000303|PubMed:26867678};
DE Short=U3-55K {ECO:0000303|PubMed:26867678};
GN Name=RRP9 {ECO:0000312|HGNC:HGNC:16829};
GN Synonyms=RNU3IP2, U355K {ECO:0000303|PubMed:26867678};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-113 AND 267-273, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Teratocarcinoma;
RX PubMed=9418896; DOI=10.1128/mcb.18.1.488;
RA Pluk H., Soffner J., Luehrmann R., van Venrooij W.J.;
RT "cDNA cloning and characterization of the human U3 small nucleolar
RT ribonucleoprotein complex-associated 55-kilodalton protein.";
RL Mol. Cell. Biol. 18:488-498(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH U3 SNRNA, AND DOMAIN.
RX PubMed=10982864; DOI=10.1093/nar/28.18.3462;
RA Lukowiak A.A., Granneman S., Mattox S.A., Speckmann W.A., Jones K.,
RA Pluk H., van Venrooij W.J., Terns R.M., Terns M.P.;
RT "Interaction of the U3-55k protein with U3 snoRNA is mediated by the box
RT B/C motif of U3 and the WD repeats of U3-55k.";
RL Nucleic Acids Res. 28:3462-3471(2000).
RN [6]
RP INTERACTION WITH U3 SNRNA.
RX PubMed=12381732; DOI=10.1074/jbc.m206631200;
RA Granneman S., Pruijn G.J.M., Horstman W., van Venrooij W.J., Luehrmann R.,
RA Watkins N.J.;
RT "The hU3-55K protein requires 15.5K binding to the box B/C motif as well as
RT flanking RNA elements for its association with the U3 small nucleolar RNA
RT in Vitro.";
RL J. Biol. Chem. 277:48490-48500(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND
RP SER-57, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-10, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-12 AND LYS-25,
RP DEACETYLATION BY SIRT7, AND MUTAGENESIS OF LYS-12 AND LYS-25.
RX PubMed=26867678; DOI=10.1038/ncomms10734;
RA Chen S., Blank M.F., Iyer A., Huang B., Wang L., Grummt I., Voit R.;
RT "SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA
RT processing.";
RL Nat. Commun. 7:10734-10734(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 118-470.
RG Structural genomics consortium (SGC);
RT "Crystal structure of RRP9 WD40 repeats.";
RL Submitted (APR-2013) to the PDB data bank.
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] GLY-8 AND GLU-342.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein
CC particle (snoRNP) thought to participate in the processing and
CC modification of pre-ribosomal RNA (pre-rRNA).
CC {ECO:0000269|PubMed:26867678}.
CC -!- SUBUNIT: Interacts specifically with the U3 small nucleolar RNA (U3
CC snoRNA) (PubMed:10982864, PubMed:12381732). Binds a sub-fragment of the
CC U3 snoRNA surrounding the B/C motif (3UBC) (PubMed:10982864,
CC PubMed:12381732). This association with the U3BC RNA is dependent on
CC the binding of a protein called 15.5K to the box B/C motif
CC (PubMed:10982864, PubMed:12381732). The association of the protein with
CC the U3BC RNA was found to be also dependent on a conserved RNA
CC structure that flanks the box B/C motif (PubMed:10982864,
CC PubMed:12381732). {ECO:0000269|PubMed:10982864,
CC ECO:0000269|PubMed:12381732}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:9418896}.
CC -!- DOMAIN: The WD domains are required for nucleolar localization and U3
CC small nucleolar RNAs binding. {ECO:0000269|PubMed:10982864}.
CC -!- PTM: Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress
CC impairs pre-rRNA processing (PubMed:26867678). Deacetylation by SIRT7
CC enhances RRP9-binding to U3 snoRNA, which is a prerequisite for pre-
CC rRNA processing (PubMed:26867678). {ECO:0000269|PubMed:26867678}.
CC -!- SIMILARITY: Belongs to the WD repeat RRP9 family. {ECO:0000305}.
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DR EMBL; AJ001340; CAA04687.1; -; mRNA.
DR EMBL; AK313696; BAG36443.1; -; mRNA.
DR EMBL; CH471055; EAW65159.1; -; Genomic_DNA.
DR EMBL; BC001113; AAH01113.1; -; mRNA.
DR EMBL; BC009879; AAH09879.1; -; mRNA.
DR EMBL; BC010048; AAH10048.1; -; mRNA.
DR EMBL; BC023662; AAH23662.2; -; mRNA.
DR CCDS; CCDS2837.1; -.
DR RefSeq; NP_004695.1; NM_004704.4.
DR PDB; 4J0W; X-ray; 1.70 A; A=137-475.
DR PDB; 4JXM; X-ray; 1.92 A; A=118-470.
DR PDB; 7MQ8; EM; 3.60 A; SG=1-475.
DR PDB; 7MQ9; EM; 3.87 A; SG=1-475.
DR PDB; 7MQA; EM; 2.70 A; SG=1-475.
DR PDBsum; 4J0W; -.
DR PDBsum; 4JXM; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; O43818; -.
DR SMR; O43818; -.
DR BioGRID; 114584; 112.
DR IntAct; O43818; 24.
DR STRING; 9606.ENSP00000232888; -.
DR iPTMnet; O43818; -.
DR PhosphoSitePlus; O43818; -.
DR SwissPalm; O43818; -.
DR BioMuta; RRP9; -.
DR DOSAC-COBS-2DPAGE; O43818; -.
DR SWISS-2DPAGE; O43818; -.
DR EPD; O43818; -.
DR jPOST; O43818; -.
DR MassIVE; O43818; -.
DR MaxQB; O43818; -.
DR PaxDb; O43818; -.
DR PeptideAtlas; O43818; -.
DR PRIDE; O43818; -.
DR ProteomicsDB; 49181; -.
DR Antibodypedia; 14210; 84 antibodies from 21 providers.
DR DNASU; 9136; -.
DR Ensembl; ENST00000232888.7; ENSP00000232888.6; ENSG00000114767.7.
DR GeneID; 9136; -.
DR KEGG; hsa:9136; -.
DR MANE-Select; ENST00000232888.7; ENSP00000232888.6; NM_004704.5; NP_004695.1.
DR UCSC; uc003dbw.3; human.
DR CTD; 9136; -.
DR DisGeNET; 9136; -.
DR GeneCards; RRP9; -.
DR HGNC; HGNC:16829; RRP9.
DR HPA; ENSG00000114767; Low tissue specificity.
DR neXtProt; NX_O43818; -.
DR OpenTargets; ENSG00000114767; -.
DR PharmGKB; PA162402176; -.
DR VEuPathDB; HostDB:ENSG00000114767; -.
DR eggNOG; KOG0299; Eukaryota.
DR GeneTree; ENSGT00940000158328; -.
DR HOGENOM; CLU_014017_1_1_1; -.
DR InParanoid; O43818; -.
DR OMA; RIWKITE; -.
DR OrthoDB; 948159at2759; -.
DR PhylomeDB; O43818; -.
DR TreeFam; TF105828; -.
DR PathwayCommons; O43818; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; O43818; -.
DR BioGRID-ORCS; 9136; 624 hits in 1089 CRISPR screens.
DR ChiTaRS; RRP9; human.
DR GeneWiki; RRP9; -.
DR GenomeRNAi; 9136; -.
DR Pharos; O43818; Tbio.
DR PRO; PR:O43818; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O43818; protein.
DR Bgee; ENSG00000114767; Expressed in gastrocnemius and 101 other tissues.
DR Genevisible; O43818; HS.
DR GO; GO:0031428; C:box C/D RNP complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0034511; F:U3 snoRNA binding; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR039241; Rrp9-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19865; PTHR19865; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; RNA-binding; rRNA processing; Ubl conjugation;
KW WD repeat.
FT CHAIN 1..475
FT /note="U3 small nucleolar RNA-interacting protein 2"
FT /id="PRO_0000051313"
FT REPEAT 144..183
FT /note="WD 1"
FT REPEAT 197..236
FT /note="WD 2"
FT REPEAT 239..278
FT /note="WD 3"
FT REPEAT 281..320
FT /note="WD 4"
FT REPEAT 322..360
FT /note="WD 5"
FT REPEAT 374..413
FT /note="WD 6"
FT REPEAT 419..460
FT /note="WD 7"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 8..40
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 24..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:26867678"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:26867678"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 113
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 8
FT /note="R -> G (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1333637065)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035887"
FT VARIANT 342
FT /note="A -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035888"
FT MUTAGEN 12
FT /note="K->Q: Mimics acetylation, leading to impaired rRNA
FT processing; when associated with Q-25."
FT /evidence="ECO:0000269|PubMed:26867678"
FT MUTAGEN 12
FT /note="K->R: Impaired acetylation, leading to promote rRNA
FT processing; when associated with R-25."
FT /evidence="ECO:0000269|PubMed:26867678"
FT MUTAGEN 25
FT /note="K->Q: Mimics acetylation, leading to impaired rRNA
FT processing; when associated with Q-12."
FT /evidence="ECO:0000269|PubMed:26867678"
FT MUTAGEN 25
FT /note="K->R: Impaired acetylation, leading to promote rRNA
FT processing; when associated with R-12."
FT /evidence="ECO:0000269|PubMed:26867678"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:4JXM"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4J0W"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4J0W"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:4J0W"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:4J0W"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4J0W"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 396..405
FT /evidence="ECO:0007829|PDB:4J0W"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 412..419
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 431..443
FT /evidence="ECO:0007829|PDB:4J0W"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:4J0W"
SQ SEQUENCE 475 AA; 51841 MW; 3CD19F66EA75B627 CRC64;
MSATAAARKR GKPASGAGAG AGAGKRRRKA DSAGDRGKSK GGGKMNEEIS SDSESESLAP
RKPEEEEEEE LEETAQEKKL RLAKLYLEQL RQQEEEKAEA RAFEEDQVAG RLKEDVLEQR
GRLQKLVAKE IQAPASADIR VLRGHQLSIT CLVVTPDDSA IFSAAKDCSI IKWSVESGRK
LHVIPRAKKG AEGKPPGHSS HVLCMAISSD GKYLASGDRS KLILIWEAQS CQHLYTFTGH
RDAVSGLAFR RGTHQLYSTS HDRSVKVWNV AENSYVETLF GHQDAVAALD ALSRECCVTA
GGRDGTVRVW KIPEESQLVF YGHQGSIDCI HLINEEHMVS GADDGSVALW GLSKKRPLAL
QREAHGLRGE PGLEQPFWIS SVAALLNTDL VATGSHSSCV RLWQCGEGFR QLDLLCDIPL
VGFINSLKFS SSGDFLVAGV GQEHRLGRWW RIKEARNSVC IIPLRRVPVP PAAGS
